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P12281 (MOEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Molybdopterin molybdenumtransferase

Short name=MPT Mo-transferase
EC=2.10.1.1
Gene names
Name:moeA
Synonyms:bisB, chlE, narE
Ordered Locus Names:b0827, JW0811
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Ref.6

Catalytic activity

Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

Cofactor

Binds 1 magnesium ion per subunit. Ref.7

Pathway

Cofactor biosynthesis; molybdopterin biosynthesis.

Subunit structure

Homodimer. Ref.7 Ref.8

Sequence similarities

Belongs to the moeA family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mobAP321733EBI-554393,EBI-1133881

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Molybdopterin molybdenumtransferase
PRO_0000170989

Secondary structure

........................................................................... 411
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12281 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 6DBBC2B4191F5951

FASTA41144,067
        10         20         30         40         50         60 
MEFTTGLMSL DTALNEMLSR VTPLTAQETL PLVQCFGRIL ASDVVSPLDV PGFDNSAMDG 

        70         80         90        100        110        120 
YAVRLADIAS GQPLPVAGKS FAGQPYHGEW PAGTCIRIMT GAPVPEGCEA VVMQEQTEQM 

       130        140        150        160        170        180 
DNGVRFTAEV RSGQNIRRRG EDISAGAVVF PAGTRLTTAE LPVIASLGIA EVPVIRKVRV 

       190        200        210        220        230        240 
ALFSTGDELQ LPGQPLGDGQ IYDTNRLAVH LMLEQLGCEV INLGIIRDDP HALRAAFIEA 

       250        260        270        280        290        300 
DSQADVVISS GGVSVGEADY TKTILEELGE IAFWKLAIKP GKPFAFGKLS NSWFCGLPGN 

       310        320        330        340        350        360 
PVSATLTFYQ LVQPLLAKLS GNTASGLPAR QRVRTASRLK KTPGRLDFQR GVLQRNADGE 

       370        380        390        400        410 
LEVTTTGHQG SHIFSSFSLG NCFIVLERDR GNVEVGEWVE VEPFNALFGG L 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis."
Nohno T., Kasai Y., Saito T.
J. Bacteriol. 170:4097-4102(1988) [PubMed: 3045084] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli."
Hasona A., Ray R.M., Shanmugam K.T.
J. Bacteriol. 180:1466-1472(1998) [PubMed: 9515915] [Abstract]
Cited for: CHARACTERIZATION.
[6]"In vitro molybdenum ligation to molybdopterin using purified components."
Nichols J.D., Rajagopalan K.V.
J. Biol. Chem. 280:7817-7822(2005) [PubMed: 15632135] [Abstract]
Cited for: FUNCTION AS MPT--MO LIGASE.
[7]"The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway."
Schrag J.D., Huang W., Sivaraman J., Smith C., Plamondon J., Larocque R., Matte A., Cygler M.
J. Mol. Biol. 310:419-431(2001) [PubMed: 11428898] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION, SUBUNIT, COFACTOR.
[8]"The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin."
Xiang S., Nichols J., Rajagopalan K.V., Schindelin H.
Structure 9:299-310(2001) [PubMed: 11525167] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21151 Genomic DNA. Translation: AAA23579.1.
U00096 Genomic DNA. Translation: AAC73914.1.
AP009048 Genomic DNA. Translation: BAA35515.1.
PIRA32352.
RefSeqNP_415348.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FC5X-ray2.20A/B1-411[»]
1G8LX-ray1.95A/B1-411[»]
1G8RX-ray2.65A/B1-411[»]
2NQKX-ray2.90A/B1-411[»]
2NQMX-ray3.00A/B1-411[»]
2NQNX-ray2.20A/B1-411[»]
2NQQX-ray2.40A/B/C/D1-411[»]
2NQRX-ray2.20A/B1-411[»]
2NQSX-ray2.50A/B1-411[»]
2NQUX-ray2.70A/B1-411[»]
2NQVX-ray2.82A/B1-411[»]
2NROX-ray2.50A/B1-411[»]
2NRPX-ray3.00A/B1-411[»]
2NRSX-ray2.80A/B1-411[»]
ProteinModelPortalP12281.
SMRP12281. Positions 5-408.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10240N.
IntActP12281. 10 interactions.
MINTMINT-1250871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000620; EBESCP00000000620; EBESCG00000000516.
EBESCT00000017967; EBESCP00000017258; EBESCG00000017023.
GeneID945454.
GenomeReviewsGene locus JW0811 in contig AP009048_GR.
Gene locus b0827 in contig U00096_GR.
KEGGecj:JW0811.
eco:b0827.
PATRIC32116857. VBIEscCol129921_0854.

Organism-specific databases

EchoBASEEB0151.
EcoGeneEG10153. moeA.

Phylogenomic databases

eggNOGCOG0303.
GeneTreeEBGT00050000011591.
HOGENOMHBG731522.
OMAVPGFDNA.
PhylomeDBP12281.
ProtClustDBPRK10680.

Enzyme and pathway databases

BioCycEcoCyc:EG10153-MONOMER.
MetaCyc:EG10153-MONOMER.

Gene expression databases

GenevestigatorP12281.

Family and domain databases

InterProIPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd.
[Graphical view]
Gene3DG3DSA:2.40.340.10. G3DSA:2.40.340.10. 1 hit.
G3DSA:3.40.980.10. MPT_bd. 1 hit.
KOK03750.
PfamPF00994. MoCF_biosynth. 1 hit.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF53218. MoCF_biosynth. 1 hit.
SSF63867. MoeA_C. 1 hit.
SSF63882. MoeA_N. 1 hit.
TIGRFAMsTIGR00177. Molyb_syn. 1 hit.
PROSITEPS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMOEA_ECOLI
AccessionPrimary (citable) accession number: P12281
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: January 25, 2012
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families